Resources

Proteomics Databases



Metabolomics Databases

• • Circular Dichroism Can Determine the Secondary Structure of Proteins

  Circular Dichroism (CD) spectroscopy is a key technique for characterizing the primary, secondary, and partial tertiary structures of proteins. 1. Circular Dichroism and Protein Primary Structure While CD spectroscopy is not commonly used to determine the primary structure of proteins, it can provide insights by detecting changes in the near-UV spectrum. Specifically, shifts in peak positions can reflect alterations in the environment of aromatic amino acids, which may aid in analyzing the protein's........

• • Proteomics Detection of Secreted Proteins

  Proteomics, a key field within bioinformatics, aims to elucidate the fundamental mechanisms of life and the functional roles of proteins in biological processes by systematically analyzing the structure and function of an organism's entire protein repertoire. Proteomic methodologies have found extensive applications in the detection and characterization of secreted proteins. Secreted proteins are those released into the extracellular environment by cells via the secretory pathway, encompassing cytokines....

• • CD Changes After Protein Aggregation

  Protein aggregation is a widely observed phenomenon in biological sciences that alters the physical and chemical properties of proteins. Circular dichroism (CD) spectroscopy serves as a vital tool for investigating protein structural changes, particularly providing insights into the secondary structural characteristics of aggregated proteins. Alterations in Secondary Structure Following Aggregation Protein aggregation often induces modifications in secondary structure, such as the transition of α-helices...

• • Is Circular Dichroism Spectroscopy Accurate Before 250 Nanometers

  When evaluating the precision and accuracy of spectroscopic measurements, several factors need to be considered, including the light source, detector, and the measurement methodology. Particularly in the ultraviolet region below 250 nanometers, technical limitations and inherent physical properties may pose challenges to achieving accurate spectra.

• • What Information About Peptides Can Be Directly Obtained From Mass Spectrometry Detection

  Mass spectrometry is a crucial analytical technique used to determine the mass and structural composition of chemical substances. In biochemistry, it is particularly useful for peptide analysis, providing insights such as: 1. Peptide Mass: By measuring their mass-to-charge ratios, mass spectrometry can determine peptide masses and deduce their amino acid sequences. 2. Peptide Fragment Ions: Secondary mass spectrometry allows for the analysis of peptide fragments, facilitating the deduction of peptide.......

• • RNA Pull-Down Mass Spectrometry Analysis

  RNA Pull Down is a widely used experimental method designed to investigate RNA-protein interactions. Mass spectrometry (MS) is a powerful and precise bioanalytical approach for identifying and characterizing the mass and sequence of proteins in complex biological samples. RNA Pull Down coupled with mass spectrometry integrates these two techniques, enabling the identification of proteins interacting with specific RNA molecules.

• • Can Protein Still Be Analyzed by Mass Spectrometry After Denaturation

  Protein denaturation involves altering the protein's structure, converting it from a functional three-dimensional form into a non-functional one. Common denaturation methods include heating, and the addition of acids, bases, or organic solvents. Although denaturation changes the three-dimensional conformation, it typically does not affect the primary structure, the amino acid sequence. Therefore, mass spectrometry remains a viable method for identifying denatured proteins.

• • How Many Microliters Are Needed for Serum Mass Spectrometry Proteomics

  In mass spectrometry-based proteomics studies, the sample volume significantly impacts the quality of the experimental results. For serum samples, the required volume depends on the analytical method employed and the sensitivity of the instrumentation. Typically, analyzing a serum sample requires between 20 and 100 microliters. Researchers should determine the exact volume needed based on their specific equipment and research objectives.

• • Cross-Linking Mass Spectrometry Sample Preparation

  Cross-linking mass spectrometry (XL-MS) is a powerful analytical tool for elucidating protein structures and interactions, with the sample preparation process being a crucial determinant of experimental success. The preparation protocol for XL-MS encompasses four main stages: protein extraction, purification, cross-linking, and preparation of cross-linked protein samples for mass spectrometry analysis.

• • Translate Protein Interactions Using IPMax

  Interacting proteins are defined as protein complexes formed through protein-protein interactions within cells, which are fundamental to key biological processes such as signal transduction, gene transcription and translation, and cell cycle regulation. IPMax leverages immunoprecipitation (IP), a widely used experimental technique for studying protein-protein interactions. This approach uses specific antibodies to isolate target proteins and their interacting partners, followed by protein mass spectrometry